Q1RMZ1: S-adenosylmethionine sensor upstream of mTORC1 (SAMTOR)

S-adenosylmethionine sensor upstream of mTORC1 (SAMTOR) is a 405-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q1RMZ1.

Gene
SAMTOR
Organism
Homo sapiens
Length
405 residues
Mean pLDDT
79.3
Model
AF-Q1RMZ1-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate56%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

S-adenosyl-L-methionine-binding protein that acts as an inhibitor of mTORC1 signaling via interaction with the GATOR1 and KICSTOR complexes (PubMed:29123071, PubMed:35776786). Acts as a sensor of S-adenosyl-L-methionine to signal methionine sufficiency to mTORC1: in presence of methionine, binds S-adenosyl-L-methionine, leading to disrupt interaction with the GATOR1 and KICSTOR complexes and promote mTORC1 signaling (PubMed:29123071, PubMed:35776786). Upon methionine starvation, S-adenosyl-L-methionine levels are reduced, thereby promoting the association with GATOR1 and KICSTOR, leading to inhibit mTORC1 signaling (PubMed:29123071, PubMed:35776786). Probably also acts as a…

Subunit structure

Interacts with the DEPDC5 subunit of the GATOR1 complex; interaction is disrupted when SAMTOR binds S-adenosyl-L-methionine (PubMed:29123071, PubMed:29590090, PubMed:35776786). Interacts with the KICSTOR complex; interaction is disrupted when SAMTOR binds S-adenosyl-L-methionine (PubMed:29123071, PubMed:35776786)

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
9O5DEM3.34 ÅA=1-405

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